Effects of body size on the diurnal activity budgets of African browsing ruminants.

We compared the diurnal activity budgets of four syntopic species of African browsing ruminant that differ widely in body size. These were concurrently studied through all phases of the seasonal cycle, in the same area, using the same methods. We tested five predictions from the literature on how body size is expected to influence the behaviour of tropical ungulates: the smallest members of the browsing ruminant guild exhibit (1) the lowest allocation of diurnal time to activity; (2) the greatest hour-to-hour variation in activity and resting time; (3) the greatest reduction in activity time during the hottest days; (4) the least change between wet and the dry seasons in the ratio of feeding: ruminating time; and (5) the greatest time budget allocation to vigilance. Prediction 1 was supported in that the smaller species spent less time being active during the day. Prediction 2 was also supported in that the smaller species were more variable in their relative allocations of time to activity and resting through successive hours of the day. Contrary to Prediction 3, however, the greatest reduction in activity with increasing temperature was found for the largest guild member. The smaller species can achieve their daily food intake requirements by feeding at night and in the cool hours of the day, while the larger species have to feed during all hours of the day and are thus more susceptible to thermoregulatory constraints on foraging. Prediction 4 was partially upheld in that the largest species (giraffe) displayed the widest variation in feeding: ruminating time through the seasonal cycle. Prediction 5 was not supported, indicating that multiple factors interact with body size in determining vigilance behaviour.

Enzyme regulation by reversible zinc inhibition: glycerol phosphate dehydrogenase as an example.

Since cellular zinc is not freely available as the inorganic ion, zinc proteins must acquire their metal from some other source. But how, when, and where they acquire it is unknown. Metallothionein can participate in the controlled delivery of zinc by binding it with high stability and by mobilizing it through a novel biochemical mechanism that critically depends on the redox activity of the zinc-sulfur bond. Thus, metallothionein activates zinc-depleted alcohol (sorbitol) dehydrogenases by glutathione-modulated zinc transfer. In addition to its catalytic, co-catalytic, and/or structural roles in a myriad of enzymes, zinc also inhibits some enzymes that are not necessarily zinc enzymes, e.g. glyceraldehyde and glycerol phosphate dehydrogenases, and aldehyde dehydrogenase. Zinc inhibits glycerol phosphate dehydrogenase with an IC(50) value of 100 nM. Zinc binding is slow at low pH, but instantaneous at high pH. Thionein, the apoprotein of metallothionein, re-activates the zinc-inhibited enzyme. Tight inhibition by zinc and activation of glycerol phosphate dehydrogenase by thionein, a biological chelating agent, provide further support that modulation of zinc binding by metallothionein and thionein is a physiological mechanism of enzyme regulation. Since glycerol phosphate dehydrogenase is a key enzyme in energy metabolism, the effect of zinc is expected to elicit significant physiological responses.